Structure of phaseolin at 2.2 A resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins

J Mol Biol. 1994 May 20;238(5):748-76. doi: 10.1006/jmbi.1994.1333.

Abstract

The refinement to 2.2 A resolution of the three-dimensional structure of the seed storage protein phaseolin from the French bean (Phaseolus vulgaris) via an alternative crystal form is described. The refined structure reveals details of the molecule hitherto unobserved and in particular we identify the structural role of conserved residues within the broader 7 S (vicilin) family of seed storage proteins. On this basis we are able to postulate a canonical model for the structure of the 7 S proteins. This model in turn provides a means for interpreting the structure of the 11 S (legumin) family of seed storage proteins, for which no X-ray diffraction data are available. The 11 S proteins are shown to bear a much closer relationship to the 7 S proteins than was previously recognized. The canonical model of the 7 S protein structure also provides a basis for proposing engineered mutations of these proteins with the goal of enhancing nutritional and functional properties.

MeSH terms

  • Amino Acid Sequence
  • Crystallography, X-Ray
  • Glycosylation
  • Hydrogen Bonding
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Structure
  • Phosphates / chemistry
  • Plant Proteins / chemistry*
  • Plant Proteins / genetics
  • Polysaccharides / chemistry
  • Protein Conformation*
  • Protein Engineering
  • Protein Structure, Secondary
  • Seed Storage Proteins
  • Seeds / chemistry*
  • Sequence Alignment
  • Solvents

Substances

  • Phosphates
  • Plant Proteins
  • Polysaccharides
  • Seed Storage Proteins
  • Solvents
  • legumin protein, plant
  • phaseolin protein, Phaseolus vulgaris
  • vicilin protein, plant